Heme oxygenase 1 (HO-1) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 1 soluble form]
1_MERPQ 6_ PDSMP 11_ QDLSE 16_ ALKEA 21_ TKEVH 26_ TQAEN 31_ AEFMR 36_ NFQKG 41_ QVTRD 46_ GFKLV 51_ MASLY 56_ HIYVA 61_ LEEEI 66_ ERNKE 71_ SPVFA 76_ PVYFP 81_ EELHR 86_ KAALE 91_ QDLAF 96_ WYGPR 101_ WQEVI 106_ PYTPA 111_ MQRYV 116_ KRLHE 121_ VGRTE 126_ PELLV 131_ AHAYT 136_ RYLGD 141_ LSGGQ 146_ VLKKI 151_ AQKAL 156_ DLPSS 161_ GEGLA 166_ FFTFP 171_ NIASA 176_ TKFKQ 181_ LYRSR 186_ MNSLE 191_ MTPAV 196_ RQRVI 201_ EEAKT 206_ AFLLN 211_ IQLFE 216_ ELQEL 221_ LTHDT 226_ KDQSP 231_ SRAPG 236_ LRQRA 241_ SNKVQ 246_ DSAPV 251_ ETPRG 256_ KPPLN 261_ TRSQA 266_ PLLRW 271_ VLTLS 276_ FLVAT 281_VAVGL
1: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:11121422, PubMed:19556236, PubMed:7703255). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed:20055707)
2: (Microbial infection) During SARS-COV-2 infection, promotes SARS-CoV-2 ORF3A-mediated autophagy but is unlikely to be required for ORF3A-mediated induction of reticulophagy
3: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron